In situ tissue regeneration approach aims to exploit the body's own biological resources and reparative capability and recruit host cells by utilizing cell-instructive biomaterials. In order to immobilize and release bioactive factors in biomaterials, it is important to engineer the load effectiveness, release kinetics and cell recruiting capabilities of bioactive molecules by using suitable bonding strategies. Stromal cell-derived factor 1α (SDF-1α) is one of the most potent chemokines for stem cell recruitment, and SDF-1α-loaded scaffolds have been used for the regeneration of many types of tissues. This review summarizes the strategies to incorporate SDF-1α into scaffolds, including direct loading or adsorption, polyion complexes, specific heparin-mediated interaction and particulate system, which may be applied to the immobilization of other chemokines or growth factors. In addition, we discuss the application of these strategies in the regeneration of tissues such as blood vessel, myocardium, cartilage and bone.

The most common biotransformation of trivalent inorganic arsenic (As(III)) is methylation to mono-, di-, and trimethylated species. Methylation is catalyzed by As(III) S-adenosylmethionine (SAM) methyltransferase (termed ArsM in microbes and AS3MT in animals). Methylarsenite (MAs(III)) is both the product of the first methylation step and the substrate of the second methylation step. When the rate of the overall methylation reaction was determined with As(III) as the substrate, the first methylation step was rapid, whereas the second methylation step was slow. In contrast, when MAs(III) was used as the substrate, the rate of methylation was as fast as the first methylation step when As(III) was used as the substrate. These results indicate that there is a slow conformational change between the first and second methylation steps. The structure of CmArsM from the thermophilic alga Cyanidioschyzon merolae sp. 5508 was determined with bound MAs(III) at 2.27 Å resolution. The methyl group is facing the solvent, as would be expected when MAs(III) is bound as the substrate rather than facing the SAM-binding site, as would be expected for MAs(III) as a product. We propose that the rate-limiting step in arsenic methylation is slow reorientation of the methyl group from the SAM-binding site to the solvent, which is linked to the conformation of the side chain of a conserved residue Tyr70.